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Testosterone Replacement, Low T, HCG, & Beyond
Testosterone and Men's Health Articles
The Dynamics of Allosteric Binding of Estradiol to SHBG
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<blockquote data-quote="madman" data-source="post: 199558" data-attributes="member: 13851"><p><strong>Figure 4. Time-resolved lifetime fluorescence spectroscopy using an extrinsic fluorescent probe, bis-ANS, demonstrates that estradiol binding significantly alters the global conformational state of the SHBG: E2 complex. Panel A shows the raw data and fits the phase delay and modulation ratio obtained at increasing estradiol concentrations titrated into a solution of 40 nM SHBG and 500 nM bis-ANS. The modulation frequencies were altered from 10 to 160 MHz to determine τphase and τmod at each SHBG: E2 ratio. The excited-state lifetime data were satisfactorily fit to the most parsimonious model of 2 emitting species where the chi-square values ranged from 0.8 to 2.1. Panels B and C show the short and long lifetime components, respectively, as a function of estradiol concentrations. Panels D and E show the change in fractional (f1 and f2) and fluorescence contribution from the bis-ANS populations exhibiting short and long singlet excited state lifetime components. Collectively, the data indicate that estradiol binding to SHBG induces a global conformational change in the protein as evidenced by the significant change in relative populations of bis-ANS species exhibiting the long and short singlet excited state lifetimes.</strong></p><p><strong>[ATTACH=full]13802[/ATTACH]</strong></p></blockquote><p></p>
[QUOTE="madman, post: 199558, member: 13851"] [B]Figure 4. Time-resolved lifetime fluorescence spectroscopy using an extrinsic fluorescent probe, bis-ANS, demonstrates that estradiol binding significantly alters the global conformational state of the SHBG: E2 complex. Panel A shows the raw data and fits the phase delay and modulation ratio obtained at increasing estradiol concentrations titrated into a solution of 40 nM SHBG and 500 nM bis-ANS. The modulation frequencies were altered from 10 to 160 MHz to determine τphase and τmod at each SHBG: E2 ratio. The excited-state lifetime data were satisfactorily fit to the most parsimonious model of 2 emitting species where the chi-square values ranged from 0.8 to 2.1. Panels B and C show the short and long lifetime components, respectively, as a function of estradiol concentrations. Panels D and E show the change in fractional (f1 and f2) and fluorescence contribution from the bis-ANS populations exhibiting short and long singlet excited state lifetime components. Collectively, the data indicate that estradiol binding to SHBG induces a global conformational change in the protein as evidenced by the significant change in relative populations of bis-ANS species exhibiting the long and short singlet excited state lifetimes. [ATTACH type="full"]13802[/ATTACH][/B] [/QUOTE]
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Testosterone Replacement, Low T, HCG, & Beyond
Testosterone and Men's Health Articles
The Dynamics of Allosteric Binding of Estradiol to SHBG
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